ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P22220


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SPE1_AVESA
Primary accession number P22220
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on August 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 53)
Name and origin of the protein
Protein name Arginine decarboxylase
Synonyms ARGDC
ADC
EC 4.1.1.19
Gene name
Name: SPE1
From
Avena sativa (Oat) [TaxID: 4498] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Pooideae; Aveneae; Avena.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 427-437.
TISSUE=Leaf;
DOI=10.1007/BF00262438; PubMed=2266946 [NCBI, ExPASy, EBI, Israel, Japan]
Bell E., Malmberg R.L.;
"Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing.";
Mol. Gen. Genet. 224:431-436(1990).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X56802; CAA40137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S12265; S12265.
3D structure databases
ModBase P22220.
Organism-specific databases
Gramene P22220; -.
Ontologies
GO
GO:0008792; Molecular function: arginine decarboxylase activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006527; Biological process: arginine catabolic process (inferred from electronic annotation from InterPro).
GO:0009446; Biological process: putrescine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0008295; Biological process: spermidine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002985; Arg_decrbxlase.
IPR000183; De-COase2.
Graphical view of domain structure.
PANTHER PTHR11482:SF3; Arg_decrbxlase; 1.
Pfam PF02784; Orn_Arg_deC_N; 1.
PF00278; Orn_DAP_Arg_deC; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001336; Arg_decrbxlase; 1.
PRINTS PR01180; ARGDCRBXLASE.
PR01179; ODADCRBXLASE.
TIGRFAMs TIGR01273; speA; 1.
PROSITE PS00878; ODR_DC_2_1; 1.
PS00879; ODR_DC_2_2; 1.
ProtoNet P22220.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Decarboxylase; Direct protein sequencing; Lyase; Magnesium; Putrescine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   607  607     Arginine decarboxylase. PRO_0000149948
REGION   290   300  11     Substrate-binding (By similarity). 
BINDING   104   104        Pyridoxal phosphate (covalent) (By similarity). 
Sequence information
Length: 607 AA [This is the length of the unprocessed precursor] Molecular weight: 66706 Da [This is the MW of the unprocessed precursor] CRC64: 757114B2C02EF8A5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAKNYGDVYH VEGWGEPYFA VNKDGHLCVR IYGRETLPGQ EIDVLSVIEQ ATSADGTGKK 

        70         80         90        100        110        120 
LQFPMILRFP DVLRHRINSL HTAFANAIKY TQYGSVYQGV FPVKVNQHKD VVQDMVHFGY 

       130        140        150        160        170        180 
DHSYGLEAGS KPELLIAMSC LTKAKPGAYL VCNGYKDSAY VALALAARAM GLNVIIVLEM 

       190        200        210        220        230        240 
EEELDIVIEE SSKLGVEPVI GVRAKLLTKI PGHFGSTAGK HGKFGLPAEK IYEVAKKLKA 

       250        260        270        280        290        300 
LNKLHWLKLL HFHVGSMIPT TDIVFKAASE ASDIYCALVK EYGVETMTTL DCGGGLGVDY 

       310        320        330        340        350        360 
DGTRSGSSDM SVAYGLEEYA SSIVQAVRLK CDYHGVPHPV LCTESGRAMA SYHSMIILEA 

       370        380        390        400        410        420 
LSAIPEPKDD EDEATTEQLH GRIRDLSSKL QPTGLSMSSH AVHIKKHGIE MYKLGKKLSK 

       430        440        450        460        470        480 
SVTTDAHTIY NYHMNLSVFS LMPDYWGIQH LFPMMPVSRL DEKPTHKATL VDVTCDSDGK 

       490        500        510        520        530        540 
VDKFIRDTET MPLHPLDPKL GGYYVAVLLT GAYQEALSNK HNLFGGPSLV RVVGTGNGGA 

       550        560        570        580        590        600 
FNVEAALLGS TTEELIGTVS YDVKQDISSV IEERARENKV WEMVEKLVES GLHTMPYLAD 


YKPPPMA 

P22220 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!